CA2093753A1 - Hexapaptide - Google Patents
HexapaptideInfo
- Publication number
- CA2093753A1 CA2093753A1 CA002093753A CA2093753A CA2093753A1 CA 2093753 A1 CA2093753 A1 CA 2093753A1 CA 002093753 A CA002093753 A CA 002093753A CA 2093753 A CA2093753 A CA 2093753A CA 2093753 A1 CA2093753 A1 CA 2093753A1
- Authority
- CA
- Canada
- Prior art keywords
- pmn
- kgagdv
- stimulated
- peptide
- ingestion
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
Links
- 150000001413 amino acids Chemical group 0.000 claims abstract description 11
- ITWQLSZTLBKWJM-YUMQZZPRSA-N Lys-Gly-Ala Chemical compound OC(=O)[C@H](C)NC(=O)CNC(=O)[C@@H](N)CCCCN ITWQLSZTLBKWJM-YUMQZZPRSA-N 0.000 claims abstract description 3
- 108010039538 alanyl-glycyl-aspartyl-valine Proteins 0.000 claims abstract description 3
- 230000027455 binding Effects 0.000 abstract description 80
- 239000003446 ligand Substances 0.000 abstract description 33
- 108010034513 leukocyte response integrin Proteins 0.000 abstract description 4
- 210000000224 granular leucocyte Anatomy 0.000 description 143
- 108090000765 processed proteins & peptides Proteins 0.000 description 103
- 108010049003 Fibrinogen Proteins 0.000 description 77
- 102000008946 Fibrinogen Human genes 0.000 description 77
- 229940012952 fibrinogen Drugs 0.000 description 77
- 230000037406 food intake Effects 0.000 description 73
- 239000011324 bead Substances 0.000 description 63
- 102000004196 processed proteins & peptides Human genes 0.000 description 38
- 108010008211 N-Formylmethionine Leucyl-Phenylalanine Proteins 0.000 description 35
- PRQROPMIIGLWRP-UHFFFAOYSA-N N-formyl-methionyl-leucyl-phenylalanin Chemical compound CSCCC(NC=O)C(=O)NC(CC(C)C)C(=O)NC(C(O)=O)CC1=CC=CC=C1 PRQROPMIIGLWRP-UHFFFAOYSA-N 0.000 description 34
- 230000000694 effects Effects 0.000 description 31
- IYMAXBFPHPZYIK-BQBZGAKWSA-N Arg-Gly-Asp Chemical compound NC(N)=NCCC[C@H](N)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(O)=O IYMAXBFPHPZYIK-BQBZGAKWSA-N 0.000 description 30
- 108010044426 integrins Proteins 0.000 description 30
- 102000006495 integrins Human genes 0.000 description 30
- 230000005764 inhibitory process Effects 0.000 description 26
- 108010039221 lysyl-glutaminyl-alanyl-glycyl-aspartyl-valine Proteins 0.000 description 19
- 239000000203 mixture Substances 0.000 description 13
- 102000016938 Catalase Human genes 0.000 description 12
- 108010053835 Catalase Proteins 0.000 description 12
- 206010057249 Phagocytosis Diseases 0.000 description 11
- 239000000872 buffer Substances 0.000 description 11
- 230000008782 phagocytosis Effects 0.000 description 11
- 102100032913 Leukocyte surface antigen CD47 Human genes 0.000 description 10
- 101710098610 Leukocyte surface antigen CD47 Proteins 0.000 description 10
- 230000001419 dependent effect Effects 0.000 description 10
- 238000000034 method Methods 0.000 description 10
- 230000003389 potentiating effect Effects 0.000 description 10
- 238000012360 testing method Methods 0.000 description 10
- 238000005406 washing Methods 0.000 description 10
- 108010085895 Laminin Proteins 0.000 description 9
- 102000007547 Laminin Human genes 0.000 description 9
- 230000004913 activation Effects 0.000 description 9
- 231100000673 dose–response relationship Toxicity 0.000 description 9
- 210000004623 platelet-rich plasma Anatomy 0.000 description 9
- 102000008100 Human Serum Albumin Human genes 0.000 description 8
- 108091006905 Human Serum Albumin Proteins 0.000 description 8
- 239000003112 inhibitor Substances 0.000 description 8
- 208000010110 spontaneous platelet aggregation Diseases 0.000 description 8
- 230000000638 stimulation Effects 0.000 description 8
- 230000002776 aggregation Effects 0.000 description 7
- 238000004220 aggregation Methods 0.000 description 7
- 210000004027 cell Anatomy 0.000 description 7
- 239000012981 Hank's balanced salt solution Substances 0.000 description 6
- 235000001014 amino acid Nutrition 0.000 description 6
- 108010072041 arginyl-glycyl-aspartic acid Proteins 0.000 description 6
- 239000003153 chemical reaction reagent Substances 0.000 description 6
- 239000004816 latex Substances 0.000 description 6
- 229920000126 latex Polymers 0.000 description 6
- 235000018102 proteins Nutrition 0.000 description 6
- 102000004169 proteins and genes Human genes 0.000 description 6
- 108090000623 proteins and genes Proteins 0.000 description 6
- 102000005962 receptors Human genes 0.000 description 6
- 108020003175 receptors Proteins 0.000 description 6
- 230000002829 reductive effect Effects 0.000 description 6
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 5
- 241001529936 Murinae Species 0.000 description 5
- 239000000853 adhesive Substances 0.000 description 5
- 230000001070 adhesive effect Effects 0.000 description 5
- 210000001616 monocyte Anatomy 0.000 description 5
- 238000010647 peptide synthesis reaction Methods 0.000 description 5
- 201000001779 Leukocyte adhesion deficiency Diseases 0.000 description 4
- 241000283973 Oryctolagus cuniculus Species 0.000 description 4
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 4
- 230000003416 augmentation Effects 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 125000000487 histidyl group Chemical class [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 4
- 230000000242 pagocytic effect Effects 0.000 description 4
- 210000001539 phagocyte Anatomy 0.000 description 4
- 238000006467 substitution reaction Methods 0.000 description 4
- -1 t-butyloxycarbonyl group Chemical group 0.000 description 4
- 239000004475 Arginine Substances 0.000 description 3
- 239000004471 Glycine Substances 0.000 description 3
- 102100037369 Nidogen-1 Human genes 0.000 description 3
- 102100023038 WD and tetratricopeptide repeats protein 1 Human genes 0.000 description 3
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- 230000005540 biological transmission Effects 0.000 description 3
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 235000014304 histidine Nutrition 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 230000002401 inhibitory effect Effects 0.000 description 3
- 210000000265 leukocyte Anatomy 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 108010008217 nidogen Proteins 0.000 description 3
- 239000012071 phase Substances 0.000 description 3
- 230000004044 response Effects 0.000 description 3
- 239000000523 sample Substances 0.000 description 3
- 230000019491 signal transduction Effects 0.000 description 3
- 239000007790 solid phase Substances 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 230000009870 specific binding Effects 0.000 description 3
- 101710125089 Bindin Proteins 0.000 description 2
- 108010067306 Fibronectins Proteins 0.000 description 2
- 102000016359 Fibronectins Human genes 0.000 description 2
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- 108010058846 Ovalbumin Proteins 0.000 description 2
- 241001494479 Pecora Species 0.000 description 2
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 238000000692 Student's t-test Methods 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 210000000170 cell membrane Anatomy 0.000 description 2
- 230000035605 chemotaxis Effects 0.000 description 2
- 230000009260 cross reactivity Effects 0.000 description 2
- 210000003743 erythrocyte Anatomy 0.000 description 2
- 150000002148 esters Chemical class 0.000 description 2
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 210000000440 neutrophil Anatomy 0.000 description 2
- 229940092253 ovalbumin Drugs 0.000 description 2
- 239000008188 pellet Substances 0.000 description 2
- 108010009779 peptide 32 Proteins 0.000 description 2
- 150000004633 phorbol derivatives Chemical class 0.000 description 2
- 239000002644 phorbol ester Substances 0.000 description 2
- 239000004033 plastic Substances 0.000 description 2
- 229920000642 polymer Polymers 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 238000012353 t test Methods 0.000 description 2
- VZQHRKZCAZCACO-PYJNHQTQSA-N (2s)-2-[[(2s)-2-[2-[[(2s)-2-[[(2s)-2-amino-5-(diaminomethylideneamino)pentanoyl]amino]propanoyl]amino]prop-2-enoylamino]-3-methylbutanoyl]amino]propanoic acid Chemical compound OC(=O)[C@H](C)NC(=O)[C@H](C(C)C)NC(=O)C(=C)NC(=O)[C@H](C)NC(=O)[C@@H](N)CCCNC(N)=N VZQHRKZCAZCACO-PYJNHQTQSA-N 0.000 description 1
- FKDJUCYAPFVUIK-GJZGRUSLSA-N (2s)-2-[[(2s)-2-[formyl(methyl)amino]-4-methylpentanoyl]amino]-3-phenylpropanoic acid Chemical compound CC(C)C[C@H](N(C)C=O)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 FKDJUCYAPFVUIK-GJZGRUSLSA-N 0.000 description 1
- UHPQFNXOFFPHJW-UHFFFAOYSA-N (4-methylphenyl)-phenylmethanamine Chemical compound C1=CC(C)=CC=C1C(N)C1=CC=CC=C1 UHPQFNXOFFPHJW-UHFFFAOYSA-N 0.000 description 1
- 108091064702 1 family Proteins 0.000 description 1
- RYHBNJHYFVUHQT-UHFFFAOYSA-N 1,4-Dioxane Chemical compound C1COCCO1 RYHBNJHYFVUHQT-UHFFFAOYSA-N 0.000 description 1
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
- CFMZSMGAMPBRBE-UHFFFAOYSA-N 2-hydroxyisoindole-1,3-dione Chemical compound C1=CC=C2C(=O)N(O)C(=O)C2=C1 CFMZSMGAMPBRBE-UHFFFAOYSA-N 0.000 description 1
- 102100022749 Aminopeptidase N Human genes 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 101800005309 Carboxy-terminal peptide Proteins 0.000 description 1
- 102000004266 Collagen Type IV Human genes 0.000 description 1
- 108010042086 Collagen Type IV Proteins 0.000 description 1
- 241000518994 Conta Species 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- QOSSAOTZNIDXMA-UHFFFAOYSA-N Dicylcohexylcarbodiimide Chemical compound C1CCCCC1N=C=NC1CCCCC1 QOSSAOTZNIDXMA-UHFFFAOYSA-N 0.000 description 1
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 1
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 1
- 102100024783 Fibrinogen gamma chain Human genes 0.000 description 1
- 229920001917 Ficoll Polymers 0.000 description 1
- 101000609762 Gallus gallus Ovalbumin Proteins 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 101000757160 Homo sapiens Aminopeptidase N Proteins 0.000 description 1
- 102000006835 Lamins Human genes 0.000 description 1
- 108010047294 Lamins Proteins 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 238000000232 Merrifield's solid-phase procedure Methods 0.000 description 1
- NQTADLQHYWFPDB-UHFFFAOYSA-N N-Hydroxysuccinimide Chemical compound ON1C(=O)CCC1=O NQTADLQHYWFPDB-UHFFFAOYSA-N 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 101000781681 Protobothrops flavoviridis Disintegrin triflavin Proteins 0.000 description 1
- 206010039491 Sarcoma Diseases 0.000 description 1
- 108010031318 Vitronectin Proteins 0.000 description 1
- 102100035140 Vitronectin Human genes 0.000 description 1
- UXZMLECYBHANRH-UHFFFAOYSA-K [B+3].[O-]C(=O)C(F)(F)F.[O-]C(=O)C(F)(F)F.[O-]C(=O)C(F)(F)F Chemical compound [B+3].[O-]C(=O)C(F)(F)F.[O-]C(=O)C(F)(F)F.[O-]C(=O)C(F)(F)F UXZMLECYBHANRH-UHFFFAOYSA-K 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 239000000556 agonist Substances 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 238000003277 amino acid sequence analysis Methods 0.000 description 1
- 229940127218 antiplatelet drug Drugs 0.000 description 1
- 239000012736 aqueous medium Substances 0.000 description 1
- 150000001483 arginine derivatives Chemical class 0.000 description 1
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 1
- 210000002469 basement membrane Anatomy 0.000 description 1
- 125000001584 benzyloxycarbonyl group Chemical group C(=O)(OCC1=CC=CC=C1)* 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 238000011095 buffer preparation Methods 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- PFKFTWBEEFSNDU-UHFFFAOYSA-N carbonyldiimidazole Chemical compound C1=CN=CN1C(=O)N1C=CN=C1 PFKFTWBEEFSNDU-UHFFFAOYSA-N 0.000 description 1
- 230000017455 cell-cell adhesion Effects 0.000 description 1
- 230000035289 cell-matrix adhesion Effects 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 229920001577 copolymer Polymers 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 239000010432 diamond Substances 0.000 description 1
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N dimethyl sulfoxide Natural products CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 1
- 108010048325 fibrinopeptides gamma Proteins 0.000 description 1
- 238000000684 flow cytometry Methods 0.000 description 1
- 238000000799 fluorescence microscopy Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 229940106780 human fibrinogen Drugs 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 239000000543 intermediate Substances 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 210000005053 lamin Anatomy 0.000 description 1
- 238000000670 ligand binding assay Methods 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 238000000386 microscopy Methods 0.000 description 1
- 239000003068 molecular probe Substances 0.000 description 1
- 239000007800 oxidant agent Substances 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 238000003359 percent control normalization Methods 0.000 description 1
- BQJRUJTZSGYBEZ-YVQNUNKESA-N phorbol 12,13-dibutanoate Chemical compound C([C@]1(O)C(=O)C(C)=C[C@H]1[C@@]1(O)[C@H](C)[C@H]2OC(=O)CCC)C(CO)=C[C@H]1[C@H]1[C@]2(OC(=O)CCC)C1(C)C BQJRUJTZSGYBEZ-YVQNUNKESA-N 0.000 description 1
- 210000002381 plasma Anatomy 0.000 description 1
- 239000000106 platelet aggregation inhibitor Substances 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000010791 quenching Methods 0.000 description 1
- 238000000163 radioactive labelling Methods 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 235000017557 sodium bicarbonate Nutrition 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000010532 solid phase synthesis reaction Methods 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000008174 sterile solution Substances 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000011550 stock solution Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 229960001134 von willebrand factor Drugs 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/745—Blood coagulation or fibrinolysis factors
- C07K14/75—Fibrinogen
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Biophysics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Hematology (AREA)
- Veterinary Medicine (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Public Health (AREA)
- Engineering & Computer Science (AREA)
- Animal Behavior & Ethology (AREA)
- General Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Pharmacology & Pharmacy (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US07/866,678 US5225531A (en) | 1992-04-09 | 1992-04-09 | Hexapeptide Lys Gly Ala Gly Asp Val |
| US07/866,678 | 1992-04-09 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2093753A1 true CA2093753A1 (en) | 1993-10-10 |
Family
ID=25348153
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002093753A Abandoned CA2093753A1 (en) | 1992-04-09 | 1993-04-08 | Hexapaptide |
Country Status (7)
Families Citing this family (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1994015958A2 (en) * | 1993-01-08 | 1994-07-21 | Tanabe Seiyaku Co., Ltd. | Peptide inhibitors of cell adhesion |
| US6139819A (en) | 1995-06-07 | 2000-10-31 | Imarx Pharmaceutical Corp. | Targeted contrast agents for diagnostic and therapeutic use |
| US6521211B1 (en) | 1995-06-07 | 2003-02-18 | Bristol-Myers Squibb Medical Imaging, Inc. | Methods of imaging and treatment with targeted compositions |
| MXPA01006499A (es) | 1998-12-23 | 2002-04-08 | Searle & Co | Metodo para utilizar un inhibidor de ciclooxigenasa-2 y un inhibidor de matriz metaloproteinasa como una terapia de combinacion en el tratamiento de neoplasia. |
| US6544750B1 (en) * | 1999-08-17 | 2003-04-08 | Thromgen, Inc. | Peptide analogs as selective inhibitors of thrombin activation of protease activated receptor 1 |
| WO2018017797A1 (en) * | 2016-07-22 | 2018-01-25 | Georgia State Universtiy Research Foundation | Monoclonal antibodies to b virus and their use for identification of b virus specific reactive peptides |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5057604A (en) * | 1988-08-03 | 1991-10-15 | Washington University | Novel monoclonal antibodies |
-
1992
- 1992-04-09 US US07/866,678 patent/US5225531A/en not_active Expired - Lifetime
-
1993
- 1993-04-08 DE DE69304409T patent/DE69304409T2/de not_active Expired - Fee Related
- 1993-04-08 EP EP93870065A patent/EP0570352B1/en not_active Expired - Lifetime
- 1993-04-08 AT AT93870065T patent/ATE142225T1/de not_active IP Right Cessation
- 1993-04-08 JP JP08208193A patent/JP3334936B2/ja not_active Expired - Fee Related
- 1993-04-08 DK DK93870065.5T patent/DK0570352T3/da active
- 1993-04-08 CA CA002093753A patent/CA2093753A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| DK0570352T3 (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 1997-02-17 |
| DE69304409D1 (de) | 1996-10-10 |
| JPH0649095A (ja) | 1994-02-22 |
| EP0570352A1 (en) | 1993-11-18 |
| EP0570352B1 (en) | 1996-09-04 |
| US5225531A (en) | 1993-07-06 |
| DE69304409T2 (de) | 1997-03-20 |
| ATE142225T1 (de) | 1996-09-15 |
| JP3334936B2 (ja) | 2002-10-15 |
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